Mario Juan Borgnia

Structural Basis of Cold and Menthol Sensing by TRPM8

This study presents cryo-EM structures and functional analyses of TRPM8 activation by cold and menthol, revealing mechanisms of cold sensing and menthol specificity.

VitriFlex: An Open-Source, Modular, and Customizable Robotic Platform for Cryo-EM Grid Preparation

VitriFlex is an open-source robotic platform for cryo-EM grid preparation that enables customizable and high-resolution grid production through modular design and programmable control.

Molecular basis of the urate transporter URAT1 inhibition by gout drugs

This study determines the cryo-EM structures of URAT1 with inhibitors and reveals their binding mechanisms and conformational changes.

Cryo-EM structures of engineered Shiga toxin-based immunogens capable of eliciting neutralizing antibodies with therapeutic potential against Hemolytic Uremic Syndrome

This paper presents cryo-EM structures of engineered Shiga toxin-based immunogens that stabilize pentamers and show interaction with neutralizing antibodies, supporting their use in a vaccine for STEC-HUS.

A higher order PUF complex is central to regulation of C. elegans germline stem cells

The paper identifies a ternary PUF complex in C. elegans that regulates germline stem cells by repressing and activating gld-1 mRNA through adjacent FBEs.

Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases

This study reports the atomic structure of mouse α-synuclein fibrils and shows they differ structurally and functionally from human fibrils linked to Parkinson's and MSA.

A humanized nanobody phage display library yields potent binders of SARS CoV-2 spike

This paper develops potent humanized nanobodies against SARS-CoV-2 spike protein, showing effectiveness against the Alpha variant and providing structural insights into their neutralization mechanism.

Structural and functional landscape of α-synuclein fibril conformations amplified from cerebrospinal fluid

The paper identifies six novel α-synuclein fibril assemblies from cerebrospinal fluid samples and shows they have distinct functional properties despite no single structural feature predicting their function.